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      Xenopus laevis M18BP1 directly binds existing CENP-A nucleosomes to promote centromeric chromatin assembly

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          Summary

          Vertebrate centromeres are epigenetically defined by nucleosomes containing the histone H3 variant, CENP-A. CENP-A nucleosome assembly requires the three-protein Mis18 complex (Mis18α, Mis18β, and M18BP1) that recruits the CENP-A chaperone HJURP to centromeres, but how the Mis18 complex recognizes centromeric chromatin is unknown. Using Xenopus egg extract, we show that direct, cell cycle-regulated binding of M18BP1 to CENP-A nucleosomes recruits the Mis18 complex to interphase centromeres to promote new CENP-A nucleosome assembly. We demonstrate that Xenopus M18BP1 binds CENP-A nucleosomes using a motif that is widely conserved except in mammals. The M18BP1 motif resembles a CENP-A nucleosome binding motif in CENP-C, and we show that CENP-C competes with M18BP1 for CENP-A nucleosome binding at centromeres. We show that both CENP-C and M18BP1 recruit HJURP to centromeres for new CENP-A assembly. This study defines cellular mechanisms for recruiting CENP-A assembly factors to existing CENP-A nucleosomes for the epigenetic inheritance of centromeres.

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          Author and article information

          Journal
          101120028
          22411
          Dev Cell
          Dev. Cell
          Developmental cell
          1534-5807
          1878-1551
          29 June 2017
          24 July 2017
          24 July 2018
          : 42
          : 2
          : 190-199.e10
          Affiliations
          [1 ]Department of Biochemistry, Stanford University, 279 Campus Drive, Beckman 409, Stanford, CA 94305
          [2 ]Department of Applied Physics, Stanford University, 348 Via Pueblo Mall, Stanford, CA 94305
          Author notes
          [* ]Correspondence to Aaron Straight, astraigh@ 123456stanford.edu
          [3]

          These authors contributed equally

          [4]

          Lead contact

          Article
          PMC5544353 PMC5544353 5544353 nihpa889192
          10.1016/j.devcel.2017.06.021
          5544353
          28743005
          1c45e220-34b7-484d-b01b-4d2185f40893
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